The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis

Hyunju Ryu, Xiao Xin Sun, Yingxiao Chen, Yanping Li, Xiaoyan Wang, Roselyn S. Dai, Hong Ming Zhu, John Klimek, Larry David, Lev M. Fedorov, Yoshiaki Azuma, Rosalie C. Sears, Mu Shui Dai

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


SUMOylation plays a crucial role in regulating diverse cellular processes including ribosome biogenesis. Proteomic analyses and experimental evidence showed that a number of nucleolar proteins involved in ribosome biogenesis are modified by SUMO. However, how these proteins are SUMOylated in cells is less understood. Here, we report that USP36, a nucleolar deubiquitinating enzyme (DUB), promotes nucleolar SUMOylation. Overexpression of USP36 enhances nucleolar SUMOylation, whereas its knockdown or genetic deletion reduces the levels of SUMOylation. USP36 interacts with SUMO2 and Ubc9 and directly mediates SUMOylation in cells and in vitro. We show that USP36 promotes the SUMOylation of the small nucleolar ribonucleoprotein (snoRNP) components Nop58 and Nhp2 in cells and in vitro and their binding to snoRNAs. It also promotes the SUMOylation of snoRNP components Nop56 and DKC1. Functionally, we show that knockdown of USP36 markedly impairs rRNA processing and translation. Thus, USP36 promotes snoRNP group SUMOylation and is critical for ribosome biogenesis and protein translation.

Original languageEnglish (US)
Article numbere50684
JournalEMBO Reports
Issue number6
StatePublished - Jun 4 2021


  • SUMOylation
  • USP36
  • deubiquitinating enzyme
  • ribosome biogenesis
  • snoRNP

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Genetics


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